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GLI1 upregulates C-JUN through a specific 130-kDa isoform.

Amable L, Gavin E, Kudo K, Meng E, Rocconi RP, Shevde LA, Reed E - Int. J. Oncol. (2013)

Bottom Line: GLI1, which has five known isoforms, is a positive transcriptional regulator in Hedgehog.Southwestern blot assay, EMSA and ChIP assays indicate that only one of five isoforms of GLI1 may be responsible for the Hedgehog link with C-JUN and thus, increased platinum-DNA adduct repair.Cancer tissues express this 130-kDa isoform at levels 6-fold higher than non-malignant tissues; and this isoform exists in abundance in six of seven ovarian cancer cell lines examined.

View Article: PubMed Central - PubMed

Affiliation: National Institute on Minority Health and Health Disparities, National Institutes of Health, Bethesda, MD 20892, USA.

ABSTRACT
The Hedgehog pathway is molecularly linked to increased resistance to cisplatin and increased repair of platinum-DNA damage, through C-JUN. GLI1, which has five known isoforms, is a positive transcriptional regulator in Hedgehog. Southwestern blot assay, EMSA and ChIP assays indicate that only one of five isoforms of GLI1 may be responsible for the Hedgehog link with C-JUN and thus, increased platinum-DNA adduct repair. Cancer tissues express this 130-kDa isoform at levels 6-fold higher than non-malignant tissues; and this isoform exists in abundance in six of seven ovarian cancer cell lines examined.

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Related in: MedlinePlus

The 130-kDa isoform of GLI1 is present in human ovary cancer specimens. (A) Seven human ovarian cancer cell lines were screened by western blotting for the presence of full-length GLI1 (160 kDa) and the 130-kDa GLI1 isoform. In all cell lines analyzed, the 130-kDa isoform of GLI1 was present. (B) Ten human ovarian specimens, seven cancer and three non-cancer, were assayed by western blotting. In all samples, the 130-kDa isoform of GLI1 was observed. (C) Graphic results of quantification of the 130-kDa protein in patient samples. Protein levels were 6-fold higher in malignant tissues.
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f4-ijo-44-03-0655: The 130-kDa isoform of GLI1 is present in human ovary cancer specimens. (A) Seven human ovarian cancer cell lines were screened by western blotting for the presence of full-length GLI1 (160 kDa) and the 130-kDa GLI1 isoform. In all cell lines analyzed, the 130-kDa isoform of GLI1 was present. (B) Ten human ovarian specimens, seven cancer and three non-cancer, were assayed by western blotting. In all samples, the 130-kDa isoform of GLI1 was observed. (C) Graphic results of quantification of the 130-kDa protein in patient samples. Protein levels were 6-fold higher in malignant tissues.

Mentions: In Fig. 4A, six additional human ovarian cancer cell lines were studied for the presence of the 130-kDa GLI1 protein: ES-2, OV-90, SKOV-3, TOV-112D, A2780, A2780-CP70 and A2780-CIS. The cisplatin-resistant cell lines, A2780-CP70 and A2780-CIS, express a higher level of the 130-kDa GLI1 isoform when compared to the parental cisplatin-sensitive A2780 cells. A2780-CP70 cells have a 1.6-fold higher and A2780-CIS a 2.7-fold higher protein level of the 130-kDa GLI1 isoform.


GLI1 upregulates C-JUN through a specific 130-kDa isoform.

Amable L, Gavin E, Kudo K, Meng E, Rocconi RP, Shevde LA, Reed E - Int. J. Oncol. (2013)

The 130-kDa isoform of GLI1 is present in human ovary cancer specimens. (A) Seven human ovarian cancer cell lines were screened by western blotting for the presence of full-length GLI1 (160 kDa) and the 130-kDa GLI1 isoform. In all cell lines analyzed, the 130-kDa isoform of GLI1 was present. (B) Ten human ovarian specimens, seven cancer and three non-cancer, were assayed by western blotting. In all samples, the 130-kDa isoform of GLI1 was observed. (C) Graphic results of quantification of the 130-kDa protein in patient samples. Protein levels were 6-fold higher in malignant tissues.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC3928471&req=5

f4-ijo-44-03-0655: The 130-kDa isoform of GLI1 is present in human ovary cancer specimens. (A) Seven human ovarian cancer cell lines were screened by western blotting for the presence of full-length GLI1 (160 kDa) and the 130-kDa GLI1 isoform. In all cell lines analyzed, the 130-kDa isoform of GLI1 was present. (B) Ten human ovarian specimens, seven cancer and three non-cancer, were assayed by western blotting. In all samples, the 130-kDa isoform of GLI1 was observed. (C) Graphic results of quantification of the 130-kDa protein in patient samples. Protein levels were 6-fold higher in malignant tissues.
Mentions: In Fig. 4A, six additional human ovarian cancer cell lines were studied for the presence of the 130-kDa GLI1 protein: ES-2, OV-90, SKOV-3, TOV-112D, A2780, A2780-CP70 and A2780-CIS. The cisplatin-resistant cell lines, A2780-CP70 and A2780-CIS, express a higher level of the 130-kDa GLI1 isoform when compared to the parental cisplatin-sensitive A2780 cells. A2780-CP70 cells have a 1.6-fold higher and A2780-CIS a 2.7-fold higher protein level of the 130-kDa GLI1 isoform.

Bottom Line: GLI1, which has five known isoforms, is a positive transcriptional regulator in Hedgehog.Southwestern blot assay, EMSA and ChIP assays indicate that only one of five isoforms of GLI1 may be responsible for the Hedgehog link with C-JUN and thus, increased platinum-DNA adduct repair.Cancer tissues express this 130-kDa isoform at levels 6-fold higher than non-malignant tissues; and this isoform exists in abundance in six of seven ovarian cancer cell lines examined.

View Article: PubMed Central - PubMed

Affiliation: National Institute on Minority Health and Health Disparities, National Institutes of Health, Bethesda, MD 20892, USA.

ABSTRACT
The Hedgehog pathway is molecularly linked to increased resistance to cisplatin and increased repair of platinum-DNA damage, through C-JUN. GLI1, which has five known isoforms, is a positive transcriptional regulator in Hedgehog. Southwestern blot assay, EMSA and ChIP assays indicate that only one of five isoforms of GLI1 may be responsible for the Hedgehog link with C-JUN and thus, increased platinum-DNA adduct repair. Cancer tissues express this 130-kDa isoform at levels 6-fold higher than non-malignant tissues; and this isoform exists in abundance in six of seven ovarian cancer cell lines examined.

Show MeSH
Related in: MedlinePlus